| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT1G16570.2 |
| Family | GT33 |
| Protein Properties | Length: 497 Molecular Weight: 55812.4 Isoelectric Point: 7.0013 |
| Chromosome | Chromosome/Scaffold: 1 Start: 5670577 End: 5673600 |
| Description | glycosyl transferase, group 1 domain containing protein, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT33 | 6 | 420 | 0 |
| RACVVVLGDLGRSPRMQYHALSLARQASFQVDIVAYGGSIPHEAVLNHPSIHIHTMAQPRFIQYFPKILYPVTLLLKAFIQFTMLLWFLFVKVPAPDIFL VQNPPSVPTLIAVKWASSWRRAAFVVDWHNFGYTLLALSLGRNNLLVSLYRWSENHYGKMATGSLCVTKAMQHELDQNWGVRAKVLYDQPPEFFRPALLE ERHELFCRVRKDLCHPIGVYDFISRELENQELNETLFTTKFNADISLKQNRPALVVSSTSWTPDENFGILLEAAVMYDRRVAARSKGSETAEISEEQHHY PNLLFIITGKGPEKEMYEEKIKRLNLRHVAFRTMWLAAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCSVSYSCIQELVKDGKNGLLFSS SSELADQLLVSNSSF | |||
| Full Sequence |
|---|
| Protein Sequence Length: 497 Download |
| MGKRGRACVV VLGDLGRSPR MQYHALSLAR QASFQVDIVA YGGSIPHEAV LNHPSIHIHT 60 MAQPRFIQYF PKILYPVTLL LKAFIQFTML LWFLFVKVPA PDIFLVQNPP SVPTLIAVKW 120 ASSWRRAAFV VDWHNFGYTL LALSLGRNNL LVSLYRWSEN HYGKMATGSL CVTKAMQHEL 180 DQNWGVRAKV LYDQPPEFFR PALLEERHEL FCRVRKDLCH PIGVYDFISR ELENQELNET 240 LFTTKFNADI SLKQNRPALV VSSTSWTPDE NFGILLEAAV MYDRRVAARS KGSETAEISE 300 EQHHYPNLLF IITGKGPEKE MYEEKIKRLN LRHVAFRTMW LAAEDYPLLL GSADLGVCLH 360 TSSSGLDLPM KVVDMFGCGL PVCSVSYSCI QELVKDGKNG LLFSSSSELA DQLLVSNSSF 420 FLKDYFTKST AEDSSNVLVF CLCEQILFKG FPGNCDALMS LKAGAMETGS SGRWATEWED 480 CAKPLITQVV SQIADS* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR00032 | argG | 4.0e-11 | 303 | 415 | 114 | + argininosuccinate synthase. argG in bacteria, ARG1 in Saccharomyces cerevisiae. There is a very unusual clustering in the alignment, with a deep split between one cohort of E. coli, H. influenzae, and Streptomyces, and the other cohort of eukaryotes, archaea, and the rest of the eubacteria [Amino acid biosynthesis, Glutamate family]. | ||
| cd01635 | Glycosyltransferase_GTB_type | 1.0e-11 | 303 | 403 | 102 | + Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. | ||
| cd03801 | GT1_YqgM_like | 2.0e-14 | 21 | 414 | 409 | + This family is most closely related to the GT1 family of glycosyltransferases and named after YqgM in Bacillus licheniformis about which little is known. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea. | ||
| PLN02275 | PLN02275 | 0 | 1 | 414 | 414 | + transferase, transferring glycosyl groups | ||
| cd03816 | GT1_ALG1_like | 0 | 2 | 486 | 487 | + This family is most closely related to the GT1 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0005739 | mitochondrion |
| GO:0009058 | biosynthetic process |
| GO:0016757 | transferase activity, transferring glycosyl groups |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAG10823.1 | 0 | 89 | 496 | 1 | 358 | AC011808_11 Putative glycosyl transferase [Arabidopsis thaliana] |
| EMBL | CBI19390.1 | 0 | 1 | 492 | 9 | 481 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_001117297.1 | 0 | 1 | 496 | 1 | 496 | glycosyl transferase family 1 protein [Arabidopsis thaliana] |
| RefSeq | NP_173105.1 | 0 | 1 | 496 | 1 | 465 | glycosyl transferase family 1 protein [Arabidopsis thaliana] |
| RefSeq | XP_002283369.1 | 0 | 1 | 491 | 124 | 595 | PREDICTED: hypothetical protein [Vitis vinifera] |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| dolichyl-diphosphooligosaccharide biosynthesis | 2.4.1.142-RXN | EC-2.4.1.142 | chitobiosyldiphosphodolichol β-mannosyltransferase |
